Supplementary data for "Novel mutation/s in the conserved region of EPSPS imparts herbicide resistance in pigeonpea"

<p><strong>Figure S1. </strong>The picture represents the binding positions of different ligands in the binding pocket of w-CcEPSPS. A. GPJ B. PEP, C. S3P, D. PEP, and S3P together, and E. GPJ and PEP together. The structural diagram and the ligand interaction clearly shows the ligand&rsquo;s individual binding site in A, B, and C and the binding of the two substrates ie., PEP and S3P in the same catalytic pocket with different binding site whereas PEP and GPJ share the same binding site in the catalytic site of CcEPSPS enzyme in the E. GPJ; Glyphosate, PEP; Phosphoenol pyruvate, S3P; Shikimate-3-phosphate.</p> <p><strong>Figure S2. </strong>Ramachandran plot representing the CcEPSPS protein structure, with each residue, plotted with their respective coordinates ie., phi and psi angles. The density of the points suggests the most prevalent secondary structure and CcEPSPS show dense right-handed ɑ helices followed by 𝛽 sheet secondary structure. The points lying in between the favorable region are defined as secondary structure areas for random coils.</p> <p><strong>Figure S3. </strong>Domain search based on Simple Modular Architecture Research Tool (SMART) (http://smart.embl.de/) revealed that the EPSPS proteins from A. pigeonpea, B. <em>Vibrio cholerae </em>and C. <em>Colwellia psychrerythraea </em>contain basic EPSP synthase domain. The Interaction network developed utilizing the STRING protein-protein database (https://string-db.org/) for D. pigeonpea, E. <em>Vibrio cholerae </em>and F. <em>Colwellia psychrerythraea </em>EPSPS proteins revealed the metabolically important EPSPS enzyme.</p> <p>&nbsp;</p>